Figure 1. DisA foci remain highly dynamic upon DNA damage in ΔrecO or ΔrecA cells. (A–F) Dynamic localization of ... Figure 1. DisA foci remain highly.

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Figure 1. DisA foci remain highly dynamic upon DNA damage in ΔrecO or ΔrecA cells. (A–F) Dynamic localization of ... Figure 1. DisA foci remain highly dynamic upon DNA damage in ΔrecO or ΔrecA cells. (A–F) Dynamic localization of DisA-GFP foci demonstrated by time-lapse microscopy from individual cells of the DisA-GFP-producing strain. Time-lapse microscopy images (400 ms intervals) from DisA-GFP-producing strains stained with DAPI (blue), FM 4–64 (red) and DisA-GFP (green) seeing as foci in unperturbed ΔaddAB ΔrecJ (A), ΔrecO (C) or ΔrecA cells (E). The corresponding movies are displayed in the Supplemental data (Movies S3, S5 and S7). Time-lapse microscopy images (400 ms intervals) from DisA-GFP-producing strains in ΔaddAB ΔrecJ (B), ΔrecO (D) or ΔrecA cells (F) upon addition of 350 μg/ml Nal at the onset of sporulation. The corresponding movies are displayed in the Supplemental data (Movies S4, S6 and S8). Selected images were chosen for demonstration. Scale bars correspond to 5 μm. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. Nucleic Acids Res, gkz219, https://doi.org/10.1093/nar/gkz219 The content of this slide may be subject to copyright: please see the slide notes for details.

Figure 2. DisA interaction with RecA Figure 2. DisA interaction with RecA. (A) Scheme of the bacterial two-hybrid assay to test DisA-RecA in vivo ... Figure 2. DisA interaction with RecA. (A) Scheme of the bacterial two-hybrid assay to test DisA-RecA in vivo interaction. (B) Bacterial two-hybrid assay shows an interaction of DisA with RecA in vivo. (C) His-tagged DisA alone (1.5 μg, lane 1) or native RecA alone (1.5 μg, lane 2) were loaded onto a 50-μl Ni<sup>2+</sup> microcolumn at room temperature in Buffer A containing 20 mM imidazole. After extensive washing, the retained protein was eluted with 50-μl Buffer A containing 1 M NaCl and 0.4 M imidazole. (D) His-tagged DisA and native RecA (1.5 μg each) were loaded onto a 50-μl Ni<sup>2+</sup> microcolumn at room temperature in Buffer A containing 20 mM imidazole in the presence or the absence of 5 mM ATP and 10 μM ssDNA. After extensive washing, the retained protein(s) was eluted with 50-μl Buffer A containing 1 M NaCl and 0.4 M imidazole. (C and D) The proteins present in the different fractions were separated by SDS-PAGE, and stained with Coomassie Blue. Western blot analysis of the protein mixtures highlighted with polyclonal anti-RecA (α-RecA) or monoclonal anti-His (α-His) antibodies was perfomed. FL, flow-through; W wash; E, elution with imidazole.The proteins present in the different fractions are indicated. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. Nucleic Acids Res, gkz219, https://doi.org/10.1093/nar/gkz219 The content of this slide may be subject to copyright: please see the slide notes for details.

Figure 3. RecA-mediated ATPase activity in the presence of DisA Figure 3. RecA-mediated ATPase activity in the presence of DisA. (A) Circular 3,199-nt ssDNA (10 μM in nt) was ... Figure 3. RecA-mediated ATPase activity in the presence of DisA. (A) Circular 3,199-nt ssDNA (10 μM in nt) was incubated with RecA (0.8 μM), DisA (0.1 or 0.2 μM) or both in buffer B containing 5 mM ATP and the ATPase activity measured for 30 min. (B) Circular ssDNA was incubated with RecA, DisA D77N or DisA ΔC290 (0.1 μM), or both in buffer B containing 5 mM ATP and the ATPase activity measured for 30 min. (C) Circular ssDNA was pre-incubated with stoichiometric SsbA (0.3 μM, 1 SsbA tetramer/33-nt) and RecO (0.2 μM, 1 RecO monomer/50-nt), and then incubated with RecA (0.8 μM, 1 RecA monomer/12-nt)), DisA (0.1 or 0.2 μM, 1 DisA monomer/100- and 50-nt) or both in buffer B containing 5 mM ATP and the ATPase activity measured for 30 min. (D) Circular ssDNA was pre-incubated with SsbA (0.3 μM) and RecO (0.2 μM), and then incubated with RecA (0.8 μM) in buffer B containing 5 mM ATP and the ATPase activity measured for 5 min. Then, DisA (0.1, 0.2 or 0.4 μM) was added and the ATPase activity measured for 25 min more. All reactions were repeated three or more times with similar results. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. Nucleic Acids Res, gkz219, https://doi.org/10.1093/nar/gkz219 The content of this slide may be subject to copyright: please see the slide notes for details.

Figure 4. DisA negatively affects recombination Figure 4. DisA negatively affects recombination. (A) Circular 3,199-nt ssDNA (10 μM) and homologous dsDNA (20 μM in nt) ... Figure 4. DisA negatively affects recombination. (A) Circular 3,199-nt ssDNA (10 μM) and homologous dsDNA (20 μM in nt) were pre-incubated or not with SsbA and then incubated with RecA and increasing DisA concentrations (doubling from 0.025 to 0.2 μM) in buffer B containing 5 mM dATP (lanes 2–11) for 60 min at 37°C. (B) The circular ssDNA and homologous linear dsDNA were pre-incubated with SsbA, RecO and then with RecA and increasing DisA (doubling from 0.025 to 0.4 μM), DisA D77N or DisA ΔC290 (doubling from 0.1 to 1.6 μM) concentrations in buffer B containing 5 mM ATP for 60 min at 37°C. (C) Circular ssDNA and homologous linear dsDNA were pre-incubated with SsbA and DisA in buffer B containing 5 mM dATP, 5 min later RecA was added, and the reaction incubated for variable time (10, 20, 30, 45 and 60 min) at 37°C. (D) Circular ssDNA and homologous linear dsDNA were pre-incubated with SsbA and RecA in buffer B containing 5 mM dATP, then DisA was added and the reaction was incubated for variable time (in min) at 37°C and separated by 0.8% agarose gel electrophoresis. The position of the bands corresponding to substrates (css, lds), intermediates (joint molecule, jm), products (nicked circular, nc) and covalently closed circular duplex DNA (cds) are indicated. C denotes the control DNA substrates. The quantification of intermediates/products indicated at the bottom is the mean of ≥3 independent experiments. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. Nucleic Acids Res, gkz219, https://doi.org/10.1093/nar/gkz219 The content of this slide may be subject to copyright: please see the slide notes for details.

Figure 5. DisA-mediated c-di-AMP synthesis is not affected by RecA·ATP Figure 5. DisA-mediated c-di-AMP synthesis is not affected by RecA·ATP. Circular ssDNA and homologous linear dsDNA were ... Figure 5. DisA-mediated c-di-AMP synthesis is not affected by RecA·ATP. Circular ssDNA and homologous linear dsDNA were incubated with increasing DisA concentrations (doubling from 0.025 to 0.4 μM) (lanes 3–7), and with SsbA and RecO (lanes 8–12), or SsbA, RecO and RecA (lanes 13–17) in buffer B containing 5 mM ATP and 0.05 μM [α-<sup>32</sup>P]-ATP for 60 min at 37°C. (A) The reaction was separated as indicated in Figure 4. In lane 1, the respective css and lds substrates (termed C) were electrophoresed. The positions of the bands corresponding to css, lds and the nc products are indicated. The percentage of recombination products (nc) is shown. Results are the mean of ≥3 independent experiments. The – denotes the absence of the indicated condition. (B) In parallel the DAC activity of DisA was measured. The reaction products were separated by TLC and quantified using ImageJ. The quantification values of relative c-di-AMP amounts are shown, and the positions of the substrate (ATP), the intermediate (pppApA) and the product (c-di-AMP) are indicated. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. Nucleic Acids Res, gkz219, https://doi.org/10.1093/nar/gkz219 The content of this slide may be subject to copyright: please see the slide notes for details.

Figure 6. Proposed mechanisms for DisA in RecA-mediated DNA damage tolerance pathways. (A) An unrepaired DNA lesion on ... Figure 6. Proposed mechanisms for DisA in RecA-mediated DNA damage tolerance pathways. (A) An unrepaired DNA lesion on the leading strand template (grey dot) causes blockage of replication fork movement. DisA regulates RecA-mediated annealing of the nascent strands, reversal of the leading and lagging daughter strands to form a HJ DNA structure. Then, DNA synthesis of the DNA complementary to the damaged site (denoted by dotted line) is followed by fork regression. (B) An unrepaired DNA lesion on the lagging strand template (grey dot) causes blockage of replication fork movement. DisA regulates RecA-mediated annealing of the nascent strands with DNA synthesis initiating from the alternative template (template switching). Removal of the lesion by a specific repair pathway then occurs. Unless provided in the caption above, the following copyright applies to the content of this slide: © The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. Nucleic Acids Res, gkz219, https://doi.org/10.1093/nar/gkz219 The content of this slide may be subject to copyright: please see the slide notes for details.